Molecular cloning and splicing isoforms of mouse p144, a homologue of CA150

Citation
M. Shimada et al., Molecular cloning and splicing isoforms of mouse p144, a homologue of CA150, J BIOCHEM, 126(6), 1999, pp. 1033-1042
Citations number
40
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOCHEMISTRY
ISSN journal
0021924X → ACNP
Volume
126
Issue
6
Year of publication
1999
Pages
1033 - 1042
Database
ISI
SICI code
0021-924X(199912)126:6<1033:MCASIO>2.0.ZU;2-K
Abstract
We previously characterized p144 bearing N-acetylglucosamine residues in a rat liver nuclear matrix fraction. Based on partial amino acid sequences of rat p144, mouse p144 cDNA was cloned and sequenced, and its amino acid seq uence was predicted. The sequence revealed that p144 is a rat homologue of CA150, which is a transcription factor involved in Tat-activated human immu nodeficiency virus type 1 transcription. The reported human CA150 consists of 1098 amino acids and has a leucine zipper-like motif in its carboxyl-reg ion. However, a clone of mouse p144 cDNA encoded a CA150 consisting of 1,03 4 amino acids. The mouse CA150 was shorter by 64 amino acids than hitherto known human CA150 and lacked the leucine zipper-like motif, We designated t he longer and shorter CA150 species as CA150a and CA150b, respectively. The partial nucleotide sequences of other mouse p144 cDNA clones were examined and it was found that some clones encode CA150a having a leucine zipper-li ke motif, It was suggested that CA150a and CA150b are splicing isoforms, Al l rat and mouse tissues examined contained transcripts for both CA150a and CA150b, Both transcripts were detected in human blood and Jurkat cells as w ell as mouse CD4(+) T-cells, which are the HIV-1-sensitive counterpart in h umans.